Calculate the Km and Vmax for DADH with this substrate. Show your work.
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- a) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) abovea) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) aboveThe standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol K
- explain in quantitative terms the circumstances under which the following reaction can porceed; L-malate + NAD+ (forward arrow) oxaloacetate + NADH + H+ delta G' standard = +29.7 KJ/mol(a) Consider the oxidation of malate to oxaloacetate by NAD*: malate + NAD+ → oxaloacetate + NADH + H+ In yeast mitochondria, where the pH = 8.1, this reaction is exergonic only at low oxaloacetate concentrations. Assuming a pH = 8.1, a temperature of 37 °C, and the steady-state concentrations given below, calculate the maximum concentration of oxaloacetate at which the reaction will still be exergonic. malate + NAD*→ oxaloacetate + NADH + H* lactate + NAD →→ pyruvate + NADH + H+ half reaction Pyruvate + 2H+ + 2e → lactate Pyruvate + CO₂ + H + 2e → malate Intracellular steady state concentrations: malate = 410 μM; NAD = 20.0 mM; pyruvate = 3.22 mM; NADH = 290 μM; AG=+29.7 kJ/mol AG¹ = +25.1 kJ/mol E° (V) - 0.190 - 0.330 lactate 1.1 mM CO₂ = 15.5 torrThe kinetics data shown in this graph are from the enzyme lactate dehydrognase, which catalyzes the redox reaction lactate + NAD* pyruvate + NADH. Calculate the Km and Vmax values with correct units 0.04 0.03 1/vo (min uM-) 0.02 Recall: 0.01 Vo = Vmax[S]/(Km + [S]) 1/vo = (K/Vmax)(1/[S]) + 1/Vmax -0.02 -0.01 0.01 0.02 0.03 0.04 0.05 0.06 0.07 1/[NAD*] (µM)
- Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potential delta E° in the table 13-7b.Consider the two half-reactions below and their standard reduction potentials. NAD+ + H+ + 2e → NADH Elo= -0.32 V a-Ketoglutarate + CO₂ + 2H+ + 2e → Isocitrate E' = -0.38 V (a) What is AE" for the spontaneous redox reaction that is, the reaction that actually occurs under standard biochemical conditions (pH 7)? (b) Which of the following statements are correct under standard biochemical conditions? i. The concentration of H+ is 1.0 M. ii. The reaction NAD+ + Isocitrate → NADH + H+ + a-Ketoglutarate + CO₂ is favor- able. iii. NAD+ accepts electrons from isocitrate. iv. The NAD → NADH reaction actually occurs in reverse. The a-ketoglutarate → isocitrate reaction occurs as written. (c) Calculate AG" for the reaction in (a). (pH 7, 25°C, pressure, 1 atm.) (d) Suppose that the actual conditions are T = 25°C, pH = 7, CO₂ = 1 atm, [a-Ketoglutarate] 10 mM, [NAD+] = 2.5 mM, and [NADH] = 0.5 mM. PAR = 2 mM, [Isocitrate] DE What is the value of AG under those conditions? (Hints: pH 7 is already…Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potential
- Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH <=> Lactate + NADH+H+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b.Calculate and compare the AGº' values for the oxidation of succinate by NAD and FAD. Use the data given in the table to find the E' of the NAD: NADH and fumarate:succinate couples, and assume that E' for the enzyme-bound FAD : FADH₂ redox + couple is nearly +0.05 V. Oxidant NAD + Fumarate Reductant NADH + H Succinate + AGO for the oxidation of succinate by NAD AGO for the oxidation of succinate by FAD: n 2 E'o (V) -0.32 T -0.03 + FAD is an oxidant, whereas NAD is a reductant. + Why is FAD rather than NAD the electron acceptor in the reaction catalyzed by succinate dehydrogenase? + The oxidation of succinate by NAD is not thermodynamically feasible. + The oxidation of succinate requires two NAD molecules but only one FAD molecule. + The electron-transport chain can regenerate FAD, but not NAD˚. kJ mol-¹ -1 kJ mol-¹Calculate the catalytic efficiency (in mM) for the uninhibited reaction based on the red line in the graph below. Note the concentration of the enzyme in the reaction is 1.55 micromolar. Velocity is in units (U), and substrate concentration is in mM. The equation of the red line is: y = 0.167x + 0.133 The equation of the blue line is: y = 0.500x + 0.133 -2 -4 -2 4 10 12 1/[S]